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Membrane-mediated disorder-to-order transition of SNAP25 flexible linker facilitates its interaction with syntaxin-1 and SNARE-complex assembly

文献类型：期刊论文

作者Jiang, Xin2,3; Zhang, Zeting2; Cheng, Kai2; Wu, Qiong2; Jiang, Ling2,3; Pielak, Gary J.1,4,5,6; Liu, Maili2,3; Li, Conggang2,3
刊名FASEB JOURNAL
出版日期2019-07-01
卷号33期号:7页码:7985-7994
ISSN号0892-6638
关键词prefusion state protein NMR intrinsically disordered region circular dichroism
DOI10.1096/fj.201802796R
英文摘要The soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex comprises synaptosome-associated protein of 25 kDa (SNAP25), syntaxin-1a (syx-1), and synaptobrevin 2, which is essential for many physiologic processes requiring membrane fusion. Several studies imply that the loop region of SNAP25 plays important roles in SNARE-complex assembly. However, why and how the flexible loop facilitates the complex assembly remains poorly understood because it is purposely deleted in almost all structural studies. By using NMR spectroscopy and circular dichroism spectropolarimetry, we characterized SNAP25 structure and interactions with other SNAREs in aqueous buffer and in the membrane. We found that the N-terminal of the SNAP25 loop region binds with membrane, and this interaction induced a disorder-to-order conformational change of the loop, resulting in enhanced interaction between the C-terminal of the SNAP25 loop and syx-1. We further proved that SNARE-complex assembly efficiency decreased when we disrupted the electrostatic interaction between C-terminal of the SNAP25 loop and syx-1, suggesting that the SNAP25 loop region facilitates SNARE-complex assembly through promoting prefusion SNARE binary complex formation. Our work elucidates the role of the flexible loop and the membrane environment in SNARE-complex assembly at the residue level, which helps to understand membrane fusion, a fundamental transport and communication process in cells.-Jiang, X., Zhang, Z., Cheng, K., Wu, Q., Jiang, L., Pielak, G. J., Liu, M., Li, C. Membrane-mediated disorder-to-order transition of SNAP25 flexible linker facilitates its interaction with syntaxin-1 and SNARE-complex assembly.
WOS关键词CYSTEINE-RICH DOMAIN ; SNAP-25 ; SYNAPTOBREVIN ; PALMITOYLATION ; PHOSPHORYLATION ; ASSOCIATION ; EXOCYTOSIS ; MECHANISM ; SUGGESTS
资助项目Ministry of Science and Technology of China[2017YFA0505400] ; Innovation Team of Hubei Province[2016CFA002] ; National Natural Sciences Foundation of China[21735005] ; National Natural Sciences Foundation of China[21575156] ; National Natural Sciences Foundation of China[21203243] ; National Natural Sciences Foundation of China[21673284] ; K. C. Wong Education Foundation ; Chinese Academy of Sciences[QYZDJ-SSW-SLH027]
WOS研究方向Biochemistry & Molecular Biology ; Life Sciences & Biomedicine - Other Topics ; Cell Biology
语种英语
出版者FEDERATION AMER SOC EXP BIOL
WOS记录号WOS:000476234700015
资助机构Ministry of Science and Technology of China ; Ministry of Science and Technology of China ; Innovation Team of Hubei Province ; Innovation Team of Hubei Province ; National Natural Sciences Foundation of China ; National Natural Sciences Foundation of China ; K. C. Wong Education Foundation ; K. C. Wong Education Foundation ; Chinese Academy of Sciences ; Chinese Academy of Sciences ; Ministry of Science and Technology of China ; Ministry of Science and Technology of China ; Innovation Team of Hubei Province ; Innovation Team of Hubei Province ; National Natural Sciences Foundation of China ; National Natural Sciences Foundation of China ; K. C. Wong Education Foundation ; K. C. Wong Education Foundation ; Chinese Academy of Sciences ; Chinese Academy of Sciences ; Ministry of Science and Technology of China ; Ministry of Science and Technology of China ; Innovation Team of Hubei Province ; Innovation Team of Hubei Province ; National Natural Sciences Foundation of China ; National Natural Sciences Foundation of China ; K. C. Wong Education Foundation ; K. C. Wong Education Foundation ; Chinese Academy of Sciences ; Chinese Academy of Sciences ; Ministry of Science and Technology of China ; Ministry of Science and Technology of China ; Innovation Team of Hubei Province ; Innovation Team of Hubei Province ; National Natural Sciences Foundation of China ; National Natural Sciences Foundation of China ; K. C. Wong Education Foundation ; K. C. Wong Education Foundation ; Chinese Academy of Sciences ; Chinese Academy of Sciences
源URL[http://ir.wipm.ac.cn/handle/112942/14700]  
专题中国科学院武汉物理与数学研究所
通讯作者Liu, Maili; Li, Conggang
作者单位1.Univ North Carolina Chapel Hill, Lineberger Comprehens Canc Ctr, Chapel Hill, NC USA
2.Chinese Acad Sci, Natl Ctr Magnet Resonance Wuhan, Wuhan Inst Phys & Math,Wuhan Natl Lab Optoelect, Key Lab Magnet Resonance Biol Syst,State Key Lab, Wuhan 430072, Hubei, Peoples R China
3.Grad Univ Chinese Acad Sci, Beijing, Peoples R China
4.Univ North Carolina Chapel Hill, Dept Biochem & Biophys, Chapel Hill, NC USA
5.Univ North Carolina Chapel Hill, Dept Chem, Chapel Hill, NC USA
6.Univ North Carolina Chapel Hill, Integrat Program Biol & Genome Sci, Chapel Hill, NC USA
推荐引用方式
GB/T 7714		 Jiang, Xin,Zhang, Zeting,Cheng, Kai,et al. Membrane-mediated disorder-to-order transition of SNAP25 flexible linker facilitates its interaction with syntaxin-1 and SNARE-complex assembly[J]. FASEB JOURNAL,2019,33(7):7985-7994.
APA Jiang, Xin.,Zhang, Zeting.,Cheng, Kai.,Wu, Qiong.,Jiang, Ling.,...&Li, Conggang.(2019).Membrane-mediated disorder-to-order transition of SNAP25 flexible linker facilitates its interaction with syntaxin-1 and SNARE-complex assembly.FASEB JOURNAL,33(7),7985-7994.
MLA Jiang, Xin,et al."Membrane-mediated disorder-to-order transition of SNAP25 flexible linker facilitates its interaction with syntaxin-1 and SNARE-complex assembly".FASEB JOURNAL 33.7(2019):7985-7994.

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来源：武汉物理与数学研究所

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